NRDD_HAEIN
ID NRDD_HAEIN Reviewed; 707 AA.
AC P43752;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Anaerobic ribonucleoside-triphosphate reductase {ECO:0000250|UniProtKB:P28903};
DE EC=1.1.98.6 {ECO:0000250|UniProtKB:P28903};
DE AltName: Full=Class III ribonucleoside-triphosphate reductase {ECO:0000250|UniProtKB:P28903};
GN Name=nrdD; OrderedLocusNames=HI_0075;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Catalyzes the conversion of ribonucleotides into
CC deoxyribonucleotides, which are required for DNA synthesis and repair.
CC {ECO:0000250|UniProtKB:P28903}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + formate + H(+) = a 2'-
CC deoxyribonucleoside 5'-triphosphate + CO2 + H2O;
CC Xref=Rhea:RHEA:51476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:61557,
CC ChEBI:CHEBI:61560; EC=1.1.98.6;
CC Evidence={ECO:0000250|UniProtKB:P28903};
CC -!- ACTIVITY REGULATION: Activated under anaerobic conditions by NrdG, a
CC tightly associated activase. Activation involves the formation of a
CC glycyl radical at Gly-682. {ECO:0000250|UniProtKB:P28903}.
CC -!- SUBUNIT: Forms a tetramer composed of two NrdD and two NrdG subunits.
CC {ECO:0000250|UniProtKB:P28903}.
CC -!- SIMILARITY: Belongs to the anaerobic ribonucleoside-triphosphate
CC reductase family. {ECO:0000305}.
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DR EMBL; L42023; AAC21751.1; -; Genomic_DNA.
DR PIR; A64047; A64047.
DR RefSeq; NP_438248.1; NC_000907.1.
DR RefSeq; WP_005693847.1; NC_000907.1.
DR AlphaFoldDB; P43752; -.
DR SMR; P43752; -.
DR STRING; 71421.HI_0075; -.
DR EnsemblBacteria; AAC21751; AAC21751; HI_0075.
DR KEGG; hin:HI_0075; -.
DR PATRIC; fig|71421.8.peg.76; -.
DR eggNOG; COG1327; Bacteria.
DR eggNOG; COG1328; Bacteria.
DR HOGENOM; CLU_002707_2_0_6; -.
DR OMA; YSYDRVP; -.
DR PhylomeDB; P43752; -.
DR BioCyc; HINF71421:G1GJ1-76-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0031250; C:anaerobic ribonucleoside-triphosphate reductase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IBA:GO_Central.
DR GO; GO:0009265; P:2'-deoxyribonucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01675; RNR_III; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR012833; NrdD.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF13597; NRDD; 1.
DR TIGRFAMs; TIGR02487; NrdD; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00850; GLY_RADICAL_1; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Metal-binding; Nucleotide-binding; Organic radical;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..707
FT /note="Anaerobic ribonucleoside-triphosphate reductase"
FT /id="PRO_0000166684"
FT DOMAIN 4..95
FT /note="ATP-cone"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT DOMAIN 584..707
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT BINDING 645
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P07071"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P07071"
FT BINDING 663
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P07071"
FT BINDING 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P07071"
FT MOD_RES 682
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 707 AA; 80233 MW; A3795F7921A6781D CRC64;
MSNFGVIKRD GSRAEFEIQR IINAIKKAAS AVNISDEFYC HQIGQEVGNE IFTRHQGEID
INQIQKIVED KLMASRYPEV ARAYIEYRHD RDLAREKRSQ LTKEIEGLIE QSNVELLNEN
ANKDAKVIPT QRDLLAGIVA KHYAKHNILP RDVVEAHEKG EIHYHDLDYA PFFPMFNCML
VDLEGMLSRG FKMGNAEIEP PKSIGTATAV TAQIIAQVAS HIYGGTTINR IDEVLSPYVQ
ISYEKHLKHA QEWNVPDVEG YAKALIEKEC FDAFQSLEYE VNTLHTSNGQ TPFVTFGFGL
GTSWQSRLIQ QAILKNRIRG LGKNHKTPVF PKLVFTIKKG LNQNKGDPNY DIKQLALECA
SKRMYPDILN YDQVVKVTGS FKAPMGCRSF LGAYEEKGHE IHDGRNNLGV VSLNLPRIAL
ESKNEEDFYR TLDERLAIAK KALMTRIARL ENTKARVAPI LYMEGACGVR LKADENVAQI
FKNGRASISL GYIGIHETIN ALYNKGHIFD DEQLREKGIA IVRHLSEAVK RWQKETGYAF
SLYSTPSENL CDRFCRLDTK KFGVIEGVTD KGYYTNSYHL DVEKKVNPYD KLDFEMTYPP
LASGGFICYG EYPNIQHNLK ALEDVWDYSY DRVPYYGTNT PIDECYECGF TGEFECTSKG
FVCPKCGNHD STKVSVTRRV CGYLGSPDAR PFNAGKQEEV KRRVKHL
